Streptococcus pneumoniae secretes a glyceraldehyde-3-phosphate dehydrogenase, which binds haemoglobin and haem.

Zelene Edith Vázquez-Zamorano, Marco Antonio González-López, María Elena Romero-Espejel, Elisa Irene Azuara-Liceaga, Mavil López-Casamichana, José de Jesús Olivares-Trejo

Index: Biometals 27(4) , 683-93, (2014)

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Abstract

Streptococcus pneumoniae is a gram positive encapsulated bacterium responsible of septicaemia and upper respiratory infections in children. This pathogen requires iron to survive in the host, which it can obtain of haemoglobin (Hb) or haem. Only two Hb-binding membrane proteins have been identified up to now. However it is unknown whether this pathogen secretes proteins in order to scavenge iron from the Hb or haem. Therefore, in order to explore these possibilities, cellular growth of S. pneumoniae was tested with several alternative iron supplies. The bacterial growth was supported with iron, Hb and haem. Additionally, S. pneumoniae expressed and secreted a protein of 38 kDa which was purified and characterized as Hb and haem-binding protein. This protein was also identified by mass spectrometry as glyceraldehyde-3-phosphate dehydrogenase. Our overall results suggest that S. pneumoniae secretes a protein capable of binding two usefull iron sources for this bacterium (Hb and haem). This protein could be playing a dynamic role in the success of the invasive and infective processes of this pathogen.